A cysteine protease ATG4B that is encoded in the genome of human. [PRO:DNx, UniProtKB:Q9Y4P1]
EC 3.4.22.-;
AUT-like 1 cysteine endopeptidase;
Autophagin-1;
Autophagy-related cysteine endopeptidase 1;
Autophagy-related protein 4 homolog B;
hAPG4B
| Timeframe | Studies on this Protein(%) | All Drugs % |
|---|---|---|
| pre-1990 | 0 (0.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 0 (0.00) | 29.6817 |
| 2010's | 3 (60.00) | 24.3611 |
| 2020's | 2 (40.00) | 2.80 |
| Drug | Taxonomy | Measurement | Average (mM) | Bioassay(s) | Publication(s) |
|---|---|---|---|---|---|
| aurintricarboxylic acid | Homo sapiens (human) | IC50 | 10.4750 | 4 | 4 |
| hypericin | Homo sapiens (human) | IC50 | 32.9500 | 2 | 2 |
| tioconazole | Homo sapiens (human) | IC50 | 1.8000 | 1 | 1 |
| zpck | Homo sapiens (human) | IC50 | 1.9650 | 2 | 2 |
| n-(4-methoxybenzyl)-n'-(5-nitro-1,3-thiazol-2-yl)urea | Homo sapiens (human) | IC50 | 1.6000 | 1 | 0 |
| benzoylacrylic acid | Homo sapiens (human) | IC50 | 580.0000 | 1 | 1 |
| nsc185058 | Homo sapiens (human) | IC50 | 51.0000 | 4 | 4 |
| ellagic acid | Homo sapiens (human) | IC50 | 4.2500 | 2 | 2 |
| benzyloxycarbonyl-phe-ala-fluormethylketone | Homo sapiens (human) | IC50 | 10.0450 | 2 | 2 |
| 3-(4-octadecyl)benzoylacrylic acid | Homo sapiens (human) | IC50 | 12.0000 | 1 | 1 |
| 3-(4-octadecyl)benzoylacrylic acid | Homo sapiens (human) | Ki | 4.6000 | 1 | 1 |
This protein enables 6 target(s):
| Target | Category | Definition |
|---|---|---|
| endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain. [http://merops.sanger.ac.uk/about/glossary.htm#ENDOPEPTIDASE] |
| cysteine-type endopeptidase activity | molecular function | Catalysis of the hydrolysis of internal, alpha-peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE, https://www.ebi.ac.uk/merops/about/glossary.shtml#ENDOPEPTIDASE] |
| protein binding | molecular function | Binding to a protein. [GOC:go_curators] |
| cysteine-type peptidase activity | molecular function | Catalysis of the hydrolysis of peptide bonds in a polypeptide chain by a mechanism in which the sulfhydryl group of a cysteine residue at the active center acts as a nucleophile. [GOC:mah, https://www.ebi.ac.uk/merops/about/glossary.shtml#CATTYPE] |
| protein-phosphatidylethanolamide deconjugating activity | molecular function | Catalysis of the reaction: [protein]-C-terminal L-amino acid-glycyl-phosphatidylethanolamide + H2O = [protein]-C-terminal L-amino acid-glycine + a 1,2-diacyl-sn-glycero-3-phosphoethanolamine. An example of this reaction is the removal of ATG8 from membranes to which it is covalently linked to a phosphatidylethanolamid via its terminal glycine residue. [PMID:22240591, PMID:22652539, PMID:28330855, PMID:2882172, PMID:28901328] |
| scaffold protein binding | molecular function | Binding to a scaffold protein. Scaffold proteins are crucial regulators of many key signaling pathways. Although not strictly defined in function, they are known to interact and/or bind with multiple members of a signaling pathway, tethering them into complexes. [GOC:BHF, GOC:sjp, PMID:10433269, Wikipedia:Scaffold_protein] |
This protein is located in 4 target(s):
| Target | Category | Definition |
|---|---|---|
| mitochondrion | cellular component | A semiautonomous, self replicating organelle that occurs in varying numbers, shapes, and sizes in the cytoplasm of virtually all eukaryotic cells. It is notably the site of tissue respiration. [GOC:giardia, ISBN:0198506732] |
| endoplasmic reticulum | cellular component | The irregular network of unit membranes, visible only by electron microscopy, that occurs in the cytoplasm of many eukaryotic cells. The membranes form a complex meshwork of tubular channels, which are often expanded into slitlike cavities called cisternae. The ER takes two forms, rough (or granular), with ribosomes adhering to the outer surface, and smooth (with no ribosomes attached). [ISBN:0198506732] |
| cytosol | cellular component | The part of the cytoplasm that does not contain organelles but which does contain other particulate matter, such as protein complexes. [GOC:hjd, GOC:jl] |
| cytoplasmic vesicle | cellular component | A vesicle found in the cytoplasm of a cell. [GOC:ai, GOC:mah, GOC:vesicles] |
This protein is active in 2 target(s):
| Target | Category | Definition |
|---|---|---|
| autophagosome membrane | cellular component | The lipid bilayer surrounding an autophagosome, a double-membrane-bounded vesicle in which endogenous cellular material is sequestered. [GOC:autophagy, GOC:isa_complete] |
| cytoplasm | cellular component | The contents of a cell excluding the plasma membrane and nucleus, but including other subcellular structures. [ISBN:0198547684] |
This protein is involved in 14 target(s):
| Target | Category | Definition |
|---|---|---|
| autophagosome assembly | biological process | The formation of a double membrane-bounded structure, the autophagosome, that occurs when a specialized membrane sac, called the isolation membrane, starts to enclose a portion of the cytoplasm. [GOC:autophagy, PMID:9412464] |
| mitophagy | biological process | The selective autophagy process in which a mitochondrion is degraded by macroautophagy. [PMID:15798367] |
| proteolysis | biological process | The hydrolysis of proteins into smaller polypeptides and/or amino acids by cleavage of their peptide bonds. [GOC:bf, GOC:mah] |
| autophagy | biological process | The cellular catabolic process in which cells digest cellular materials, such as organelles and other macromolecular constituents, or non-self materials such as intracellular pathogens. Autophagy serves to provide essential nutrients under conditions of cellular stress; or can remodel intracellular structures during cell differentiation. [GOC:autophagy, ISBN:0198547684, PMID:11099404, PMID:29455577, PMID:9412464] |
| protein transport | biological process | The directed movement of proteins into, out of or within a cell, or between cells, by means of some agent such as a transporter or pore. [GOC:ai] |
| macroautophagy | biological process | The autophagic process that proceeds via the formation of an autophagosome. [PMID:24366339] |
| microautophagy | biological process | A type of autophagy where cytosolic components are ingested by late endosomes, lysosomes or yeast-type lytic vacuoles by direct invagination of the compartment membrane without prior sequestration into an autophagosome. The engulfing membranes fuse, resulting in the lysosomal delivery of the cargo wrapped in a single membrane derived from the invaginated lysosomal membrane. [PMID:14679207, PMID:15798367, PMID:16973210, PMID:9566964] |
| otolith mineralization completed early in development | biological process | The formation of otoliths during embryogenesis with completion in early postembryonic development. Formation occurs by precipitation of specific crystal forms of calcium carbonate around an organic core of extracellular matrix proteins. Otoconia (otoliths) are small (~10 micron) dense extracellular particles present in the otolith end organs of the vertebrate inner ear. [GOC:dsf, PMID:15581873] |
| protein localization to phagophore assembly site | biological process | Any process in which a protein is transported to, or maintained at, the phagophore assembly site (PAS). [GOC:rb] |
| protein delipidation | biological process | The breakage of covalent bonds to detach lipid groups from a protein. [GOC:ai] |
| protein processing | biological process | Any protein maturation process achieved by the cleavage of a peptide bond or bonds within a protein. Protein maturation is the process leading to the attainment of the full functional capacity of a protein. [GOC:curators, GOC:jl, GOC:jsg] |
| piecemeal microautophagy of the nucleus | biological process | Degradation of a cell nucleus by microautophagy. [GOC:autophagy, GOC:jp, PMID:18701704] |
| aggrephagy | biological process | The selective degradation of protein aggregates by macroautophagy. [GOC:autophagy, GOC:kmv, PMID:18508269, PMID:25062811] |
| C-terminal protein lipidation | biological process | The covalent attachment of a lipid group to the carboxy-terminus of a protein. [GOC:jl] |